ID   GLGS_BRANA              Reviewed;         520 AA.
AC   Q9M462;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic;
DE            EC=2.7.7.27;
DE   AltName: Full=ADP-glucose pyrophosphorylase;
DE   AltName: Full=ADP-glucose synthase;
DE   AltName: Full=AGPase B;
DE   AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
DE   Flags: Precursor;
GN   Name=AGPS1;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Drakkar; TISSUE=Seed;
RA   Zawodny S., Martini N.;
RT   "Isolation and analysis of a cDNA clone encoding the small subunit of ADP-
RT   glucose pyrophosphorylase in the plastids of seeds and leaves of Oilseed
RT   rape (Brassica napus).";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein plays a role in synthesis of starch. It
CC       catalyzes the synthesis of the activated glycosyl donor, ADP-glucose
CC       from Glc-1-P and ATP.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose
CC         + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498,
CC         ChEBI:CHEBI:58601; EC=2.7.7.27;
CC   -!- ACTIVITY REGULATION: Activated by 3'phosphoglycerate, inhibited by
CC       orthophosphate. Allosteric regulation.
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SUBUNIT: Heterotetramer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Leaves.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
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DR   EMBL; AJ271162; CAB89863.1; -; mRNA.
DR   RefSeq; NP_001303131.1; NM_001316202.1.
DR   AlphaFoldDB; Q9M462; -.
DR   SMR; Q9M462; -.
DR   PRIDE; Q9M462; -.
DR   EnsemblPlants; CDY27884; CDY27884; GSBRNA2T00038740001.
DR   GeneID; 106366674; -.
DR   Gramene; CDY27884; CDY27884; GSBRNA2T00038740001.
DR   KEGG; bna:106366674; -.
DR   OMA; ISKDAMM; -.
DR   UniPathway; UPA00152; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR011831; ADP-Glc_PPase.
DR   InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR43523; PTHR43523; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR02091; glgC; 1.
DR   PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR   PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR   PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; ATP-binding; Chloroplast; Nucleotide-binding;
KW   Nucleotidyltransferase; Plastid; Starch biosynthesis; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..71
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           72..520
FT                   /note="Glucose-1-phosphate adenylyltransferase small
FT                   subunit, chloroplastic"
FT                   /id="PRO_0000011151"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  57045 MW;  D0EAFC9706F3B6A7 CRC64;
     MATMAAIGSL KVPSSSSNHT RRLSSSSQRK TLSFSSSSLT GEKLNPTQEI IISNLPRGNE
     RRTPSIVSPK AVSDSQNSQT CLDPDASRSV LGIILGGGAG TRLYPLTKKR AKPAVPLGAN
     YRLIDIPVSN CLNSNISKIY VLTQFNSASL NRHLSRAYAS NMGGYKNEGF VEVLAAQQSP
     ENPNWFQGTA DAVRQYLWLF EEHNVLEFLV LAGDHLYRMD YEKFIQAHRE TDADITVAAL
     PMDEKRATAF GLMKIDDEGR IIEFAEKPKG EQLKAMKVDT TILGLDDERA KEMPFIASMG
     IYVVSKNVML DLLRDQFPGA NDFGSEVIPG ATDLGLRVQA YLYDGYWEDI GTIEAFYNAN
     LGITKKPVPD FSFYDRSAPI YTQPRYLPPS KMLDADVTDS VIGEGCVIKN CKIHHSVIGL
     RSCISEGAII EDTLLMGADY YETDADRTLL AAKGSIPIGI GRDSHIKRAI IDKNARIGDN
     VKIINTDNVQ EAARETDGYF IKSGIVTVIK DALIPSGTVI